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dc.contributor.authorDupree, Paulen
dc.date.accessioned2017-10-03T12:32:57Z
dc.date.available2017-10-03T12:32:57Z
dc.date.issued2017-10-20en
dc.identifier.issn2041-1723
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/267689
dc.description.abstractLytic polysaccharide monooxygenases (LPMOs) are industrially important copper-dependent enzymes that oxidatively cleave polysaccharides. We studied two closely related AA9-family LPMOs from Lentinus similis (LsAA9A) and Collariella virescens (CvAA9A). LsAA9A and CvAA9A cleave a range of polysaccharides, including cellulose, xyloglucan, mixed-linkage glucan, and glucomannan. LsAA9A additionally cleaves isolated xylan substrates, the first LPMO to show such activity. Insights into the determinants of specificity come from the structures of CvAA9A and of LsAA9A bound to cellulosic and non-cellulosic oligosaccharides. EPR spectra further reveal differences in copper co-ordination on binding of xylan compared to glucans. LsAA9A activity is notably less sensitive to reducing agent potential on xylan when compared to other substrates, suggesting a different mechanistic pathway for the cleavage of xylan. These data show that AA9 LPMOs can display different apparent substrate specificities dependent upon both productive protein:carbohydrate interactions across a binding surface and also electronic considerations at the copper active site.
dc.description.sponsorshipTravel to synchrotrons was supported by the Danish Ministry of Higher Education and Science through the Instrument Center DANSCATT and the European Community’s Seventh Framework Programme (FP7/2007-2013) under BioStruct-X (grant agreement 283570). This work was supported by the UK Biotechnology and Biological Sciences Research Council (grant numbers BB/L000423/1 to P.D. and P.H.W., and BB/L021633/1 to P.H.W.) and the Danish Council for Strategic Research (grant numbers 12-134923 to L.L.L. and 12-134922 to K.S.J.).
dc.publisherNature Publishing Group
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rightsAttribution 4.0 Internationalen
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.titleStructural and electronic determinants of lytic polysaccharide monooxygenase reactivity on polysaccharide substratesen
dc.typeArticle
prism.number1064en
prism.publicationDate2017en
prism.publicationNameNature Communicationsen
prism.volume8en
dc.identifier.doi10.17863/CAM.13622
dcterms.dateAccepted2017-08-29en
rioxxterms.versionofrecord10.1038/s41467-017-01247-3en
rioxxterms.versionAM*
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/en
rioxxterms.licenseref.startdate2017-10-20en
dc.contributor.orcidDupree, Paul [0000-0001-9270-6286]
dc.identifier.eissn2041-1723
rioxxterms.typeJournal Article/Reviewen
pubs.funder-project-idBBSRC (via University of York) (R1500502)
pubs.funder-project-idBBSRC (BB/G016240/1)
pubs.funder-project-idBBSRC (via Rothamsted Research) (unknown)
pubs.funder-project-idBBSRC (via University of York) (R15011 BB/L001926/1)
pubs.funder-project-idBiotechnology and Biological Sciences Research Council (BB/L000423/1)
cam.issuedOnline2017-10-20en
cam.orpheus.successThu Jan 30 13:00:12 GMT 2020 - The item has an open VoR version.*
rioxxterms.freetoread.startdate2100-01-01


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International